|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05469 |
PRK05469 |
tripeptide aminopeptidase PepT; |
2-409 |
0e+00 |
|
tripeptide aminopeptidase PepT;
Pssm-ID: 235484 [Multi-domain] Cd Length: 408 Bit Score: 722.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 2 YENLLPRFLRYVKTETRSDATSTTTPSTQTQVAFAQTLKKELEELGMSDVIYNEtNGFVIATLPSNVEKDVRSIGFIAHM 81
Cdd:PRK05469 1 MDKLLERFLRYVKIDTQSDENSTTVPSTEGQWDLAKLLVEELKELGLQDVTLDE-NGYVMATLPANVDKDVPTIGFIAHM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 82 DTA-DFNAVNVSPQIVENYDGeSTIPLDKEGkFTLNTKDFPNLKNYRGETLITTDGTTLLGADDKSGIAEIMTAMEYLIN 160
Cdd:PRK05469 80 DTApDFSGKNVKPQIIENYDG-GDIALGDGN-EVLSPAEFPELKNYIGQTLITTDGTTLLGADDKAGIAEIMTALEYLIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 161 HPEIKHGTIRVAFGPDEEIGVGADKFDVAQFNVDFAYTMDGGPVGELQFETFNAAQAEITIQGKNVHPGTAKNTMINALQ 240
Cdd:PRK05469 158 HPEIKHGDIRVAFTPDEEIGRGADKFDVEKFGADFAYTVDGGPLGELEYENFNAASAKITIHGVNVHPGTAKGKMVNALL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 241 LGIDFHNALPADEVPEKTAGEEGFYHLAAFAGTPEEATMTYIIRDHNREIFEARKAKIKEIQQTLNAPFDEERIKVDLFD 320
Cdd:PRK05469 238 LAADFHAMLPADETPETTEGYEGFYHLTSIKGTVEEAELSYIIRDFDREGFEARKALMQEIAKKVNAKYGEGRVELEIKD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 321 QYYNMREVIEKDMSIVEIAKQAMEELSIQPIIEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRFEFVSLQAMEKATNVI 400
Cdd:PRK05469 318 QYYNMREKIEPHPHIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMGLPCPNIFTGGHNFHGKFEFVSLESMEKAVEVI 397
|
....*....
gi 488289220 401 IKIAELNAK 409
Cdd:PRK05469 398 VEIAELTAE 406
|
|
| M20_peptT |
cd03892 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; ... |
5-406 |
0e+00 |
|
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; tripeptide aminopeptidase; tripeptidase) subfamily. PepT acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349887 [Multi-domain] Cd Length: 400 Bit Score: 658.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 5 LLPRFLRYVKTETRSDATSTTTPSTQTQVAFAQTLKKELEELGMSDVIYNEtNGFVIATLPSNVEKDVRSIGFIAHMDTA 84
Cdd:cd03892 1 LLERFLRYVKIDTQSDESSETVPSTEGQLELAKLLAKELKELGLEDVTLDE-HGYVTATLPANVDKDVPTIGFIAHMDTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 85 DFN-AVNVSPQIVENYDGEStIPLDKEGkFTLNTKDFPNLKNYRGETLITTDGTTLLGADDKSGIAEIMTAMEYLINHPE 163
Cdd:cd03892 80 PDNsGKNVKPQIIENYDGGD-IVLNESG-IVLSPAEFPELKNYKGQTLITTDGTTLLGADDKAGIAEIMTALEYLIEHPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 164 IKHGTIRVAFGPDEEIGVGADKFDVAQFNVDFAYTMDGGPVGELQFETFNAAQAEITIQGKNVHPGTAKNTMINALQLGI 243
Cdd:cd03892 158 IKHGDIRVGFTPDEEIGRGADHFDVEKFGADFAYTLDGGELGELEYENFNAASATITITGVNVHPGTAKGKMVNALLLAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 244 DFHNALPADEVPEKTAGEEGFYHLAAFAGTPEEATMTYIIRDHNREIFEARKAKIKEIQQTLNAPFDEERIKVDLFDQYY 323
Cdd:cd03892 238 DFHSMLPREETPEHTEGYEGFYHLLSMEGTVEEAELSYIIRDFDRDGFEARKELIKEIAKKLNAKYGEGRVELEIKDQYY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 324 NMREVIEKDMSIVEIAKQAMEELSIQPIIEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRFEFVSLQAMEKATNVIIKI 403
Cdd:cd03892 318 NMKEKIEPHMHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNFHGRYEFVPVESMEKAVEVIVKI 397
|
...
gi 488289220 404 AEL 406
Cdd:cd03892 398 AEL 400
|
|
| peptidase-T |
TIGR01882 |
peptidase T; This model represents a tripeptide aminopeptidase known as Peptidase T, which has ... |
2-408 |
0e+00 |
|
peptidase T; This model represents a tripeptide aminopeptidase known as Peptidase T, which has a substrate preference for hydrophobic peptides. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 130937 [Multi-domain] Cd Length: 410 Bit Score: 611.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 2 YENLLPRFLRYVKTETRSDATSTTTPSTQTQVAFAQTLKKELEELGMSDVIYNETNGFVIATLPSNVEKDVRSIGFIAHM 81
Cdd:TIGR01882 2 YEELLPRFLTYVKVNTRSDENSDTCPSTPGQLTFGNMLVDDLKSLGLQDAHYDEKNGYVIATIPSNTDKDVPTIGFLAHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 82 DTADFNAVNVSPQIVENYDGESTIPLDkEGKFTLNTKDFPNLKNYRGETLITTDGTTLLGADDKSGIAEIMTAMEYLINH 161
Cdd:TIGR01882 82 DTADFNGENVNPQIIENYDGESIIQLG-DLEFTLDPDQFPNLSGYKGQTLITTDGTTLLGADDKAGIAEIMTAADYLINH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 162 PEIKHGTIRVAFGPDEEIGVGADKFDVAQFNVDFAYTMDGGPVGELQFETFNAAQAEITIQGKNVHPGTAKNTMINALQL 241
Cdd:TIGR01882 161 PEIKHGTIRVAFTPDEEIGRGAHKFDVKDFNADFAYTVDGGPLGELEYETFSAAAAKITIQGNNVHPGTAKGKMINAAQI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 242 GIDFHNALPADEVPEKTAGEEGFYHLAAFAGTPEEATMTYIIRDHNREIFEARKAKIKEIQQTLNAPFDEERIKVDLFDQ 321
Cdd:TIGR01882 241 AIDLHNLLPEDDRPEYTEGREGFFHLLSIDGTVEEAKLHYIIRDFEKENFQERKELMKRIVEKMNNEYGQDRIKLDMNDQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 322 YYNMREVIEKDMSIVEIAKQAMEELSIQPIIEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRFEFVSLQAMEKATNVII 401
Cdd:TIGR01882 321 YYNMAEKIEKVMEIVDIAKQAMENLGIEPKISPIRGGTDGSQLSYMGLPTPNIFAGGENMHGRFEYISVDNMVKAVDVIV 400
|
....*..
gi 488289220 402 KIAELNA 408
Cdd:TIGR01882 401 EIAKLNE 407
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
3-409 |
9.61e-169 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 478.26 E-value: 9.61e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 3 ENLLPRFLRYVKTETRSDATSTTTPSTQTQVAFAQTLKKELEELGMSDvIYNETNGFVIATLPSNVEkDVRSIGFIAHMD 82
Cdd:PRK13381 1 MQLTDRFFRYLKVNSQSDAASGTLPSTPGQHELAKLLADELRELGLED-IVIDEHAIVTAKLPGNTP-GAPRIGFIAHLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 83 TADFNAV-NVSPQIVEnYDGEStIPLDKEGKFTLNTKDFPNLKNYRGETLITTDGTTLLGADDKSGIAEIMTAMEYLINH 161
Cdd:PRK13381 79 TVDVGLSpDIHPQILR-FDGGD-LCLNAEQGIWLRTAEHPELLNYQGEDIIFSDGTSVLGADNKAAIAVVMTLLENLTEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 162 pEIKHGTIRVAFGPDEEIGV-GADKFDVAQFNVDFAYTMDGGPVGELQFETFNAAQAEITIQGKNVHPGTAKNTMINALQ 240
Cdd:PRK13381 157 -EVEHGDIVVAFVPDEEIGLrGAKALDLARFPVDFAYTIDCCELGEVVYENFNAASAEITITGVTAHPMSAKGVLVNPIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 241 LGIDFHNALPADEVPEKTAGEEGFYHLAAFAGTPEEATMTYIIRDHNREIFEARKAKIKEIQQTLNAPFDEERIKVDLFD 320
Cdd:PRK13381 236 MANDFISHFPRQETPEHTEGREGYIWVNDLQGNVNKAKLKLIIRDFDLDGFEARKQFIEEVVAKINAKYPTARVSLTLTD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 321 QYYNMREVIEKDMSIVEIAKQAMEELSIQPIIEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRFEFVSLQAMEKATNVI 400
Cdd:PRK13381 316 QYSNISNSIKDDRRAVDLAFDAMKELGIEPKVIPMRGGTDGAALSAKGLPTPNLFTGAHNFHSRFEFLPVSSFVKSYEVT 395
|
....*....
gi 488289220 401 IKIAELNAK 409
Cdd:PRK13381 396 ITICLLAAK 404
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
1-408 |
3.15e-166 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 470.30 E-value: 3.15e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 1 MYENLLPRFLRYVKTETRSDATStttpstqtqvAFAQTLKKELEELGMsDVIYNEtNGFVIATLPSNVEKDVRSIGFIAH 80
Cdd:COG2195 1 NPERLLERFLEYVKIPTPSDHEE----------ALADYLVEELKELGL-EVEEDE-AGNVIATLPATPGYNVPTIGLQAH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 81 MDTA-DFNAVNVSPQIvenyDGEstipldkegkftlntkdfpnlknyrgetLITTDGTTLLGADDKSGIAEIMTAMEYLI 159
Cdd:COG2195 69 MDTVpQFPGDGIKPQI----DGG----------------------------LITADGTTTLGADDKAGVAAILAALEYLK 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 160 nHPEIKHGTIRVAFGPDEEIG-VGADKFDVAQFNVDFAYTMDGGPVGELQFETFNAAQAEITIQGKNVHPGTAKNTMINA 238
Cdd:COG2195 117 -EPEIPHGPIEVLFTPDEEIGlRGAKALDVSKLGADFAYTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 239 LQLGIDFHNALPADEVPEKTAGEEGFYHL-AAFAGTPEEATMTYIIRDHNREIFEARKAKIKEIQQTLNAPFDEERIKVD 317
Cdd:COG2195 196 IKLAARFLAALPLGRIPEETEGNEGFIHGgSATNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGVGVVEVE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 318 LFDQYYNMREviEKDMSIVEIAKQAMEELSIQPIIEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRFEFVSLQAMEKAT 397
Cdd:COG2195 276 IEDQYPNWKP--EPDSPIVDLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAW 353
|
410
....*....|.
gi 488289220 398 NVIIKIAELNA 408
Cdd:COG2195 354 ELLVEILKLIA 364
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
5-406 |
1.22e-115 |
|
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; tripeptide aminopeptidase; tripeptidase) subfamily and similar proteins. PepT acts only on tripeptide substrates, and is thus termed a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349897 [Multi-domain] Cd Length: 400 Bit Score: 343.20 E-value: 1.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 5 LLPRFLRYVKTETRSDATSTTTPSTQTQVAFAQTLKKELEELGMSDVIYNETnGFVIATLPSNVEKDVRSIGFIAHMDTA 84
Cdd:cd05645 1 LLERFLEYVSLDTQSKAGVRQVPSTEGQWKLLKLLKKQLEELGLINVTLSEK-GTLIATLPANVDGDIPAIGFISHVDTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 85 -DFNAVNVSPQIVENYDGESTIPldKEGKFTLNTKDFPNLKNYRGETLITTDGTTLLGADDKSGIAEIMTAMEYLINHPe 163
Cdd:cd05645 80 pDGSGKNVNPQIVENYRGGDIAL--GIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGLAEIFTALAVLKEKN- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 164 IKHGTIRVAFGPDEEIGVGADKFDVAQFNVDFAYTMDGGPVGELQFETFNAAQAEITIQGKNVHPGTAKNTMINALQLGI 243
Cdd:cd05645 157 IPHGDIEVAFTPDEEVGKGAKHFDVEAFTAKWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVGVNALSLAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 244 DFHNALPADEVPEKTAGEEGFYHLAAFAGTPEEATMTYIIRDHNREIFEARKAKIKEIQQTLNAPFDEE-RIKVDLFDQY 322
Cdd:cd05645 237 RIHAEVPADESPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDFDRKQFEARKRK*KEIAKKVGKGLHPDcYIELVIEDSY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 323 YNMREVIEKDMSIVEIAKQAMEELSIQPIIEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRFEFVSLQAMEKATNVIIK 402
Cdd:cd05645 317 YNFREKVVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLEGLEKAVQVIVR 396
|
....
gi 488289220 403 IAEL 406
Cdd:cd05645 397 IAEL 400
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
35-405 |
3.26e-39 |
|
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349932 [Multi-domain] Cd Length: 368 Bit Score: 144.13 E-value: 3.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 35 FAQTLKKELEELGMSDVIYN--ETNGF----VIATLPSNVEkDVRSIGFIAHMDTadfnavnVSPqivenydGESTIPLD 108
Cdd:cd05683 25 ISKVLKKKFENLGLSVIEDDagKTTGGgagnLICTLKADKE-EVPKILFTSHMDT-------VTP-------GINVKPPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 109 KEGKFtlntkdfpnlknyrgetlITTDGTTLLGADDKSGIAEIMTAMEYlINHPEIKHGTIRVAFGPDEEIG-VGADKFD 187
Cdd:cd05683 90 IADGY------------------IYSDGTTILGADDKAGIAAILEAIRV-IKEKNIPHGQIQFVITVGEESGlVGAKALD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 188 VAQFNVDFAYTMDG-GPVGELQFETFNAAQAEITIQGKNVHPGTAKNTMINALQLGIDFHNALPADEVPEKTAGEEGFYH 266
Cdd:cd05683 151 PELIDADYGYALDSeGDVGTIIVGAPTQDKINAKIYGKTAHAGTSPEKGISAINIAAKAISNMKLGRIDEETTANIGKFQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 267 laafAGTPeeatmTYIIRDHNREIFEAR-------KAKIKEIQQTLNAPFDEERIKVDL-FDQYYNMREVIEKDmSIVEI 338
Cdd:cd05683 231 ----GGTA-----TNIVTDEVNIEAEARsldeeklDAQVKHMKETFETTAKEKGAHAEVeVETSYPGFKINEDE-EVVKL 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488289220 339 AKQAMEELSIQPIIEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRFEFVSLQAMEKATNVIIKIAE 405
Cdd:cd05683 301 AKRAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLYDTAVLVVEIIK 367
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
34-405 |
8.80e-38 |
|
peptidase T-like protein; This model represents a clade of enzymes closely related to Peptidase T, an aminotripeptidase found in bacteria. This clade consists of gram positive bacteria of which several additionally contain a Peptidase T gene.
Pssm-ID: 162579 [Multi-domain] Cd Length: 361 Bit Score: 140.07 E-value: 8.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 34 AFAQTLKKELEELGMS----DVIYNETNGF-VIATLPSNVEKDvrSIGFIAHMDTADfNAVNVSPQIVENYdgestipld 108
Cdd:TIGR01883 21 AILTYLKKQITKLGIPvsldEVPAEVSNDNnLIARLPGTVKFD--TIFFCGHMDTVP-PGAGPEPVVEDGI--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 109 kegkftlntkdfpnlknyrgetlITTDGTTLLGADDKSGIAEIMTAMEYLiNHPEIKHGTIRVAFGPDEEIG-VGADKFD 187
Cdd:TIGR01883 89 -----------------------FTSLGGTILGADDKAGVAAMLEAMDVL-STEETPHGTIEFIFTVKEELGlIGMRLFD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 188 VAQFNVDFAYTMD-GGPVGELQFETFNAAQAEITIQGKNVHPGTAKNTMINALQLGIDFHNALPADEVPEKTAGEEGFYh 266
Cdd:TIGR01883 145 ESKITAAYGYCLDaPGEVGNIQLAAPTQVKVDATIAGKDAHAGLVPEDGISAISVARMAIHAMRLGRIDEETTANIGSF- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 267 laafagtpEEATMTYIIRDHNREIFEARKAKIKEIQ---QTLNAPFDEE------RIKVDLFDQYYNMRevIEKDMSIVE 337
Cdd:TIGR01883 224 --------SGGVNTNIVQDEQLIVAEARSLSFRKAEaqvQTMRERFEQAaekygaTLEEETRLIYEGFK--IHPQHPLMN 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289220 338 IAKQAMEELSIQPIIEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRFEFVSLQAMEKATNVIIKIAE 405
Cdd:TIGR01883 294 IFKKAAKKIGLKTSEIFSGGGSDANVLNEKGVPTVNLSAGYVHAHTEKETISIEQLVKLAELVIALAE 361
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
36-405 |
2.82e-23 |
|
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 100.34 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 36 AQTLKKELEELGMSDVIYNETNGF--VIATLPSNVEKdvRSIGFIAHMDTadfnavnVSPqivENYDGESTIPldkegkF 113
Cdd:COG0624 35 AELLAELLEALGFEVERLEVPPGRpnLVARRPGDGGG--PTLLLYGHLDV-------VPP---GDLELWTSDP------F 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 114 TLntkdfpnlknyrgetliTTDGTTLLG---ADDKSGIAEIMTAMEYLINHPEIKHGTIRVAFGPDEEIG-VGADKF--- 186
Cdd:COG0624 97 EP-----------------TIEDGRLYGrgaADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGsPGARALvee 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 187 DVAQFNVDFAYTMDGGPVGELQFETFNAAQAEITIQGKNVHPGTAkNTMINALQLGIDFHNALPADEVPEKTAGEEGFYH 266
Cdd:COG0624 160 LAEGLKADAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAHSSRP-ELGVNAIEALARALAALRDLEFDGRADPLFGRTT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 267 LAA---FAGT-----PEEATMTYIIR---DHNREIFEARkakikeIQQTLNAPFDEERIKVDLFDQYYN-MRevIEKDMS 334
Cdd:COG0624 239 LNVtgiEGGTavnviPDEAEAKVDIRllpGEDPEEVLAA------LRALLAAAAPGVEVEVEVLGDGRPpFE--TPPDSP 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289220 335 IVEIAKQAMEELS-IQPIIEPVRGGTDGSKIS-YLGIPTPNI-FAGGENMHGRFEFVSLQAMEKATNVIIKIAE 405
Cdd:COG0624 311 LVAAARAAIREVTgKEPVLSGVGGGTDARFFAeALGIPTVVFgPGDGAGAHAPDEYVELDDLEKGARVLARLLE 384
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
142-405 |
1.13e-20 |
|
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 91.64 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 142 ADDKSGIAEIMTAMEYLINHPeIKHGTIRVAFGPDEEIGVG-----ADKFDVAQFNVDFAYTMD----GGPVGELQFETF 212
Cdd:pfam01546 33 DDMKGGLLAALEALRALKEEG-LKKGTVKLLFQPDEEGGMGgaralIEDGLLEREKVDAVFGLHigepTLLEGGIAIGVV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 213 NA----AQAEITIQGKNVH---PGTAKN------TMINALQlGIDFHNALPADEVPeKTAGEEGFYHlAAFAGTPEEATM 279
Cdd:pfam01546 112 TGhrgsLRFRVTVKGKGGHastPHLGVNaivaaaRLILALQ-DIVSRNVDPLDPAV-VTVGNITGIP-GGVNVIPGEAEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 280 TYIIRDHNREIFEARKAKIKEIqqtLNAPFDEERIKVDlFDQYYNMREVIEKDMSIVEIAKQAMEEL---SIQPIIEPVR 356
Cdd:pfam01546 189 KGDIRLLPGEDLEELEERIREI---LEAIAAAYGVKVE-VEYVEGGAPPLVNDSPLVAALREAAKELfglKVELIVSGSM 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 488289220 357 GGTDGSKISyLGIPtPNIF---AGGENMHGRFEFVSLQAMEKATNVIIKIAE 405
Cdd:pfam01546 265 GGTDAAFFL-LGVP-PTVVffgPGSGLAHSPNEYVDLDDLEKGAKVLARLLL 314
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
36-404 |
4.46e-14 |
|
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like; Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline.
Pssm-ID: 349944 [Multi-domain] Cd Length: 361 Bit Score: 73.10 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 36 AQTLKKELEELGM---SDVIYNETNgfVIATLPSNVEkdvRSIGFIAHMDTadfnavnVSPQiveNYDGESTIPL---DK 109
Cdd:cd08659 20 AEYLAELLAKRGYgieSTIVEGRGN--LVATVGGGDG---PVLLLNGHIDT-------VPPG---DGDKWSFPPFsgrIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 110 EGKFtlntkdfpnlknyRGetlittdgttlLGADD-KSGIAEIMTAMEYLINHPEIKHGTIRVAFGPDEEIG-VGADKFD 187
Cdd:cd08659 85 DGRL-------------YG-----------RGACDmKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGsDGARALL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 188 vaqfNVDFAYTMDGGPVGE-LQFETFNAA----QAEITIQGKNVHpGTAKNTMINALQLGIDFHNALpADEVPEKTAGEE 262
Cdd:cd08659 141 ----EAGYADRLDALIVGEpTGLDVVYAHkgslWLRVTVHGKAAH-SSMPELGVNAIYALADFLAEL-RTLFEELPAHPL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 263 gfyhLAAF--------AGT-----PEEATMTYIIR---DHNREIFearkakIKEIQQTLNAPFDEERIKVDLFDQYYnmr 326
Cdd:cd08659 215 ----LGPPtlnvgvinGGTqvnsiPDEATLRVDIRlvpGETNEGV------IARLEAILEEHEAKLTVEVSLDGDPP--- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 327 EVIEKDMSIVEIAKQAMEELSIQPIIEPVRGGTDGSKIS-YLGIPTPnIFAGGEN--MHGRFEFVSLQAMEKATNVIIKI 403
Cdd:cd08659 282 FFTDPDHPLVQALQAAARALGGDPVVRPFTGTTDASYFAkDLGFPVV-VYGPGDLalAHQPDEYVSLEDLLRAAEIYKEI 360
|
.
gi 488289220 404 A 404
Cdd:cd08659 361 I 361
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
36-394 |
2.88e-12 |
|
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.
Pssm-ID: 349881 [Multi-domain] Cd Length: 362 Bit Score: 67.62 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 36 AQTLKKELEELGMS-DVIYNETNG-FVIATLPSNVEKDvrsIGFIAHMDTAdfnavnvspqivenydgestipldkegkf 113
Cdd:cd03885 25 AELLAEELEALGFTvERRPLGEFGdHLIATFKGTGGKR---VLLIGHMDTV----------------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 114 tlntkdFPnlKNYRGETLITTDGTTLLG---ADDKSGIAEIMTAMEYLINHPEIKHGTIRVAFGPDEEIG---------V 181
Cdd:cd03885 73 ------FP--EGTLAFRPFTVDGDRAYGpgvADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGspgsrelieE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 182 GADKFDVAqFNVDFAytmdgGPVGELQFETFNAAQAEITIQGKNVHPGtakntmiNALQLGIdfhNALpaDEVPEKTage 261
Cdd:cd03885 145 EAKGADYV-LVFEPA-----RADGNLVTARKGIGRFRLTVKGRAAHAG-------NAPEKGR---SAI--YELAHQV--- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 262 EGFYHLAAFA------------GT-----PEEATMTYIIRDHNREIFEARKAKIKEIQQTlnAPFDEERIKVDLFDQYYN 324
Cdd:cd03885 204 LALHALTDPEkgttvnvgvisgGTrvnvvPDHAEAQVDVRFATAEEADRVEEALRAIVAT--TLVPGTSVELTGGLNRPP 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289220 325 MREViEKDMSIVEIAKQAMEELSIQPIIEPVRGGTDGSKISYLGIPTPNIF-AGGENMHGRFEFVSLQAME 394
Cdd:cd03885 282 MEET-PASRRLLARAQEIAAELGLTLDWEATGGGSDANFTAALGVPTLDGLgPVGGGAHTEDEYLELDSLV 351
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
39-399 |
4.35e-12 |
|
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 67.04 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 39 LKKELEELGMS-DVI-----YNETNGFVIATLPSNveKDVRSIGFIAHMDTadfnavnVSPQIVENYDGESTIPLDKEGK 112
Cdd:TIGR01910 27 IKDLLREFGFStDVIeitddRLKVLGKVVVKEPGN--GNEKSLIFNGHYDV-------VPAGDLELWKTDPFKPVEKDGK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 113 FtlntkdfpnlknY-RGETlittdgttllgaDDKSGIAEIMTAMEYLINHPEIKHGTIRVAFGPDEEIG-VGADKF--DV 188
Cdd:TIGR01910 98 L------------YgRGAT------------DMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGeAGTLYLlqRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 189 AQFNVDFAYTMDGGPVGELQFETFNAAQAEITIQGKNVHPGTAkNTMINALQLGIDFHNALpADEVPEKTAG-EEGFYHL 267
Cdd:TIGR01910 154 YFKDADGVLIPEPSGGDNIVIGHKGSIWFKLRVKGKQAHASFP-QFGVNAIMKLAKLITEL-NELEEHIYARnSYGFIPG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 268 AAFAGT------------PEEATMTYIIRDHNREIFEARKAKIKEIQQTLNAP---FDEERIKVDLFDQYYnmrevIEKD 332
Cdd:TIGR01910 232 PITFNPgvikggdwvnsvPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSKSdgwLYENEPVVKWSGPNE-----TPPD 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289220 333 MSIVEIAKQAMEE-LSIQPIIEPVRGGTDGSKISYLGIPTPNIFAG-GENMHGRFEFVSLQAMEKATNV 399
Cdd:TIGR01910 307 SRLVKALEAIIKKvRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPGdLETAHQVNEYISIKNLVESTKV 375
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
148-360 |
1.86e-10 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 61.85 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 148 IAEIMTAMEYLINHPEIKHGTIRVAFGPDEEIGVGAdKFDVAQ-----FNVDFAY---TMDGGPVGELQFE--TFNAA-- 215
Cdd:cd03886 94 TAMLLGAAKLLAERRDPLKGTVRFIFQPAEEGPGGA-KAMIEEgvlenPGVDAAFglhVWPGLPVGTVGVRsgALMASad 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 216 QAEITIQGKNVHPGTAKNTmINALQLGIDFHNAL---PADEVPEKTAGEEGFYHLAafAGT-----PEEATMTYIIRDHN 287
Cdd:cd03886 173 EFEITVKGKGGHGASPHLG-VDPIVAAAQIVLALqtvVSRELDPLEPAVVTVGKFH--AGTafnviPDTAVLEGTIRTFD 249
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289220 288 REIFEARKAKIKEIQQTLNAPFDEErIKVDLFDQYynmrEVIEKDMSIVEIAKQAMEELSIQP---IIEPVRGGTD 360
Cdd:cd03886 250 PEVREALEARIKRLAEGIAAAYGAT-VELEYGYGY----PAVINDPELTELVREAAKELLGEEavvEPEPVMGSED 320
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
143-405 |
2.59e-10 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 61.31 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 143 DDKSGIAEIMTAMEYLinHPEIKHGTIRVAFGPDEEIGVGADKFDVAQFNVDFAYTMDggPV-GELQFETFNAAQAEITI 221
Cdd:PRK08652 87 DAKGGVAAILLALEEL--GKEFEDLNVGIAFVSDEEEGGRGSALFAERYRPKMAIVLE--PTdLKVAIAHYGNLEAYVEV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 222 QGKNVHpGTAKNTMINALQLGIDFHNALPADEvPEKTAGEEGFYHLAAFAGTPEEatmtYIIRDHNREIFEAR---KAKI 298
Cdd:PRK08652 163 KGKPSH-GACPESGVNAIEKAFEMLEKLKELL-KALGKYFDPHIGIQEIIGGSPE----YSIPALCRLRLDARippEVEV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 299 KEIQQTLNAPFDEERIKVDLFDQYYNMreVIEKDMSIVEIAKQAMEELSIQPIIEPVRGGTDGSKISYLGIPTPnIFAGG 378
Cdd:PRK08652 237 EDVLDEIDPILDEYTVKYEYTEIWDGF--ELDEDEEIVQLLEKAMKEVGLEPEFTVMRSWTDAINFRYNGTKTV-VWGPG 313
|
250 260
....*....|....*....|....*....
gi 488289220 379 E--NMHGRFEFVSLQAMEKATNVIIKIAE 405
Cdd:PRK08652 314 EldLCHTKFERIDVREVEKAKEFLKALNE 342
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
209-311 |
4.61e-10 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 56.59 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 209 FETFNAAQAEITIQGKNVHPGtAKNTMINALQLGIDFHNALPAD----------EVPEKTAGEEGFyhlaAFAGTPEEAT 278
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSG-APGKGVNAIKLLARLLAELPAEygdigfdfprTTLNITGIEGGT----ATNVIPAEAE 75
|
90 100 110
....*....|....*....|....*....|...
gi 488289220 279 MTYIIRdhnREIFEARKAKIKEIQQTLNAPFDE 311
Cdd:pfam07687 76 AKFDIR---LLPGEDLEELLEEIEAILEKELPE 105
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
60-208 |
1.27e-09 |
|
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 57.44 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 60 VIATLPSNVEKdvRSIGFIAHMDTadfnavnvspqivenydgestIPLDKEGkftlNTKDFPNlknyrGETLITTDGTTL 139
Cdd:cd03873 2 LIARLGGGEGG--KSVALGAHLDV---------------------VPAGEGD----NRDPPFA-----EDTEEEGRLYGR 49
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289220 140 LGADDKSGIAEIMTAMEYLINHPEIKHGTIRVAFGPDEEIGVGADKFDVAQ------FNVDFAYTMDGGPVGELQ 208
Cdd:cd03873 50 GALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEEVGSGGGKGLLSKfllaedLKVDAAFVIDATAGPILQ 124
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
60-204 |
6.06e-09 |
|
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 55.52 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 60 VIATLPSNVEKdvRSIGFIAHMDTadfnavnvspqivenydgestIPLDKEGkftlNTKDFPNlknyrGETLITTDGTTL 139
Cdd:cd18669 2 VIARYGGGGGG--KRVLLGAHIDV---------------------VPAGEGD----PRDPPFF-----VDTVEEGRLYGR 49
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289220 140 LGADDKSGIAEIMTAMEYLINHPEIKHGTIRVAFGPDEEIGVGADKF------DVAQFNVDFAYTMDGGPV 204
Cdd:cd18669 50 GALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEEVGSGAGKGllskdaLEEDLKVDYLFVGDATPA 120
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
142-400 |
3.74e-08 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 55.00 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 142 ADDKSGIAEIMTAMEYLInhpEIKHGTIRVAFGPDEEI-GVGAdkfdvAQFNVDFAYTMDGGPVGELQFETF--NAA--- 215
Cdd:PRK08651 113 SDMKGGIAALLAAFERLD---PAGDGNIELAIVPDEETgGTGT-----GYLVEEGKVTPDYVIVGEPSGLDNicIGHrgl 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 216 -QAEITIQGKNVHPGTAkNTMINALQLGIDFHNAL---------------PADEVPEKTAGEEgfyhlAAFAGT-----P 274
Cdd:PRK08651 185 vWGVVKVYGKQAHASTP-WLGINAFEAAAKIAERLksslstikskyeyddERGAKPTVTLGGP-----TVEGGTktnivP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 275 EEATMTYIIR----DHNREIFEARKAKIKEIQQTLNAPFdeERIKVDLFDQYYnmrevIEKDMSIVEIAKQAMEE-LSIQ 349
Cdd:PRK08651 259 GYCAFSIDRRlipeETAEEVRDELEALLDEVAPELGIEV--EFEITPFSEAFV-----TDPDSELVKALREAIREvLGVE 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 488289220 350 PIIEPVRGGTDGSKISYLGIPTPNIFAGGENM-HGRFEFVSLQAMEKATNVI 400
Cdd:PRK08651 332 PKKTISLGGTDARFFGAKGIPTVVYGPGELELaHAPDEYVEVKDVEKAAKVY 383
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
152-360 |
5.08e-07 |
|
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441082 [Multi-domain] Cd Length: 386 Bit Score: 51.27 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 152 MTAMEYLINHPEIKHGTIRVAFGPDEEIGVGADK------FDvaQFNVDFAYT---MDGGPVGELQF--ETFNAA--QAE 218
Cdd:COG1473 110 LGAAKALAELRDELKGTVRLIFQPAEEGGGGAKAmiedglLD--RPDVDAIFGlhvWPGLPVGTIGVrpGPIMAAadSFE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 219 ITIQGKNVH---PGTAKNT------MINALQlgidfhnALPADEVPektAGEEGFYHLAAF-AGT-----PEEATMTYII 283
Cdd:COG1473 188 ITIKGKGGHaaaPHLGIDPivaaaqIVTALQ-------TIVSRNVD---PLDPAVVTVGIIhGGTapnviPDEAELEGTV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 284 RDHNREIFEARKAKIKEIQQTLNAPFDEErIKVDLFDQY---YNmreviekDMSIVEIAKQAMEELSIQPII---EPVRG 357
Cdd:COG1473 258 RTFDPEVRELLEERIERIAEGIAAAYGAT-AEVEYLRGYpptVN-------DPELTELAREAAREVLGEENVvdaEPSMG 329
|
...
gi 488289220 358 GTD 360
Cdd:COG1473 330 SED 332
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
142-239 |
1.10e-06 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 50.40 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 142 ADDKSGIAEIMTAMEYLINHPEIKHGTIRVAFGPDEEIG-VGADKF---DVAQFNVDFAYTmDGGPVGELQFETFNAAQA 217
Cdd:PRK06133 135 ADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGsPGSRELiaeLAAQHDVVFSCE-PGRAKDALTLATSGIATA 213
|
90 100
....*....|....*....|..
gi 488289220 218 EITIQGKNVHPGTAKNTMINAL 239
Cdd:PRK06133 214 LLEVKGKASHAGAAPELGRNAL 235
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
152-380 |
9.14e-06 |
|
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273857 [Multi-domain] Cd Length: 363 Bit Score: 47.34 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 152 MTAMeYLINHPEIKHGTIRVAFGPDEEIGVGADKF--DVAQFNVDFAYTM---DGGPVGELQFE--TFNAA--QAEITIQ 222
Cdd:TIGR01891 100 GTAK-LLKKLADLLEGTVRLIFQPAEEGGGGATKMieDGVLDDVDAILGLhpdPSIPAGTVGLRpgTIMAAadKFEVTIH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 223 GKNVH---PGTAKNTMINALQLGIDFHNALPAdEVPektAGEEGFYHLAAF-AGT-----PEEATMTYIIRDHNREIFEA 293
Cdd:TIGR01891 179 GKGAHaarPHLGRDALDAAAQLVVALQQIVSR-NVD---PSRPAVVSVGIIeAGGapnviPDKASMSGTVRSLDPEVRDQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 294 RKAKIKEIQQTLNAPFdeeRIKVDL-FDQYYnmrEVIEKDMSIVEIAKQAMEE----LSIQPIIEPVRGGTDGSKISYLg 368
Cdd:TIGR01891 255 IIDRIERIVEGAAAMY---GAKVELnYDRGL---PAVTNDPALTQILKEVARHvvgpENVAEDPEVTMGSEDFAYYSQK- 327
|
250
....*....|..
gi 488289220 369 IPTPNIFAGGEN 380
Cdd:TIGR01891 328 VPGAFFFLGIGN 339
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
151-360 |
1.65e-05 |
|
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349939 [Multi-domain] Cd Length: 365 Bit Score: 46.51 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 151 IMTAMEYLINHPEIKHGTIRVAFGPDEEIGVGADKF--DVAQFNVDFAYTMDGGPVGELQFETFNAA-------QAEITI 221
Cdd:cd08018 95 VLGAAELLKKIGLVKKGKLKFLFQPAEEKGTGALKMieDGVLDDVDYLFGVHLRPIQELPFGTAAPAiyhgastFLEGTI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 222 QGKNVHpGTAKNTMINALQLGIDFHNALPADEV-PEKT---------AGEEgfyhlaAFAGTPEEATMTYIIRDHNREIF 291
Cdd:cd08018 175 KGKQAH-GARPHLGINAIEAASAIVNAVNAIHLdPNIPwsvkmtklqAGGE------ATNIIPDKAKFALDLRAQSNEAM 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289220 292 EARKAKIKEIQQTLNAPFDeerIKVDLFDQYYNMREVIEKDMsiVEIAKQAM-----EELSIQPIIEPvrGGTD 360
Cdd:cd08018 248 EELKEKVEHAIEAAAALYG---ASIEITEKGGMPAAEYDEEA--VELMEEAItevlgEEKLAGPCVTP--GGED 314
|
|
| M20_Acy1-like |
cd05666 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
167-360 |
9.99e-05 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349916 [Multi-domain] Cd Length: 373 Bit Score: 44.05 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 167 GTIRVAFGPDEEIGVGADK------FDvaQFNVDFAY---TMDGGPVGELQFET--FNAA--QAEITIQGKNVH------ 227
Cdd:cd05666 114 GTVHFIFQPAEEGGGGAKAmiedglFE--RFPCDAVYglhNMPGLPAGKFAVRPgpMMASadTFEITIRGKGGHaamphl 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 228 ---PGTAKNTMINALQlGIDFHNALPAD----EVPEKTAGEegfyhlaAFAGTPEEATMTYIIR---DHNREIFEARkak 297
Cdd:cd05666 192 gvdPIVAAAQLVQALQ-TIVSRNVDPLDaavvSVTQIHAGD-------AYNVIPDTAELRGTVRafdPEVRDLIEER--- 260
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488289220 298 IKEIQQTLNAPFDEErIKVDLFDQYynmrEVIEKDMSIVEIAKQAMEEL----SIQPIIEPVRGGTD 360
Cdd:cd05666 261 IREIADGIAAAYGAT-AEVDYRRGY----PVTVNDAEETAFAAEVAREVvgaeNVDTDVRPSMGSED 322
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
148-386 |
1.94e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349940 [Multi-domain] Cd Length: 372 Bit Score: 43.09 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 148 IAEIMTAMEYLINHPEIKHGTIRVAFGPDEEIGVGADKF--DVAQFNVDFAYTM---DGGPVGELQFE---TF-NAAQAE 218
Cdd:cd08019 93 TAMLLGAAKILNEIKDTIKGTVKLIFQPAEEVGEGAKQMieEGVLEDVDAVFGIhlwSDVPAGKISVEagpRMaSADIFK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 219 ITIQGKNVHPGTAKNTmINALQLGIDFHNALPADEVPEKTAGEEGFYHLAAF-AGT-----PEEATMTYIIRDHNREIFE 292
Cdd:cd08019 173 IEVKGKGGHGSMPHQG-IDAVLAAASIVMNLQSIVSREIDPLEPVVVTVGKLnSGTrfnviADEAKIEGTLRTFNPETRE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 293 ARKAKIKEIQQTLNAPFdeeRIKVDLfdQYYNMREVIEKDMSIVEIAKQAMEELSIQPIIEPVRGGTDGSKISY------ 366
Cdd:cd08019 252 KTPEIIERIAKHTAASY---GAEAEL--TYGAATPPVINDEKLSKIARQAAIKIFGEDSLTEFEKTTGSEDFSYyleevp 326
|
250 260
....*....|....*....|....*
gi 488289220 367 -----LGIPTPNIFAGGENMHGRFE 386
Cdd:cd08019 327 gvfafVGSRNEEKGATYPHHHEFFN 351
|
|
| M20_Acy1-like |
cd05668 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
154-292 |
5.04e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial uncharacterized proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349918 [Multi-domain] Cd Length: 371 Bit Score: 42.13 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 154 AMEYLINHPeiKHGTIRVAFGPDEEIGVGAD------KFdvAQFNVDFAYTMD---GGPVGELQFET--FNAAQ--AEIT 220
Cdd:cd05668 105 GMELSQNRP--QKGKVILLFQPAEETGEGAAaviadpKF--KEIQPDFAFALHnlpGLELGQIAVKKgpFNCASrgMIIR 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 221 IQGKNVHPGTAKNTMINALQLG--IDFHNALPaDEVPEKT--------AGEegfyhlAAFAGTPEEATMTYIIRDHNREI 290
Cdd:cd05668 181 LKGRTSHAAHPEAGVSPAEAMAklIVALPALP-DAMPKFTlvtvihakLGE------AAFGTAPGEATVMATLRAHTNET 253
|
..
gi 488289220 291 FE 292
Cdd:cd05668 254 ME 255
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
117-187 |
6.06e-04 |
|
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear.
Pssm-ID: 349885 [Multi-domain] Cd Length: 474 Bit Score: 41.74 E-value: 6.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289220 117 TKDFpnLKNYRGETLITTDGTTLlGADDKSGIAEIMTAMEylinHPEIKHGTIRVAFGPDEEIG-VGADKFD 187
Cdd:cd03890 84 EKDP--IKLRIDGDWLKATGTTL-GADNGIGVAYALAILE----DKDIEHPPLEVLFTVDEETGmTGALGLD 148
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
143-236 |
1.12e-03 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 41.08 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 143 DDKSGIAEIMTAMEYLINH---PEikhGTIRVAFGPDEEI-GVGADKfdVAQF----NVDFAYTMD-GGPVGElqfetfn 213
Cdd:PRK08262 154 DDKGSLVAILEAAEALLAQgfqPR---RTIYLAFGHDEEVgGLGARA--IAELlkerGVRLAFVLDeGGAITE------- 221
|
90 100
....*....|....*....|...
gi 488289220 214 aaqaeitiqgkNVHPGTAKNTMI 236
Cdd:PRK08262 222 -----------GVLPGVKKPVAL 233
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
135-215 |
4.60e-03 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 39.16 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289220 135 DGTTLLG---ADDKSGIAEIMTAMEYLI-NHPEIKHgTIRVAFGPDEEIG--VGA---DKFDVAQFNVD-FAYTMD-GGP 203
Cdd:cd05674 101 DGGYIWGrgaLDDKNSLIGILEAVELLLkRGFKPRR-TIILAFGHDEEVGgeRGAgaiAELLLERYGVDgLAAILDeGGA 179
|
90
....*....|..
gi 488289220 204 VGELQFETFNAA 215
Cdd:cd05674 180 VLEGVFLGVPFA 191
|
|
| |
